1r2q

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(New page: 200px<br /> <applet load="1r2q" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r2q, resolution 1.05Å" /> '''Crystal Structure o...)
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Revision as of 16:52, 12 November 2007

Image:1r2q.gif

Crystal Structure of Human Rab5a GTPase Domain at 1.05 A resolution

Overview

Rab5 is a GTPase that regulates early endosome fusion. Its GTPase domain, crystal structure is reported here at 1.05 A resolution in complex with a, GTP-analog molecule. It provides the highest resolution three-dimensional, model so far obtained for proteins from the Ras-like GTPase family. This, study allows extension of structural examination of the GTPase machinery, as well as of high-resolution protein structures in general. For example, a buried water-molecule network was observed underneath the switch, regions, which is consistent with the functional roles of these regions in, the molecular-switching process. Furthermore, residues of multiple, conformation and clustered distribution of anisotropic thermal motions of, the protein molecule may have general implications for the function of, Ras-like GTPases.

About this Structure

1R2Q is a Single protein structure of sequence from Homo sapiens with MG, GNP and GOL as ligands. Full crystallographic information is available from OCA.

Reference

Refinement of the structure of human Rab5a GTPase domain at 1.05 A resolution., Terzyan S, Zhu G, Li G, Zhang XC, Acta Crystallogr D Biol Crystallogr. 2004 Jan;60(Pt 1):54-60. Epub 2003, Dec 18. PMID:14684892

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